Evidence map›Paper›PMID 25750911›Full record

ReviewFrontiers in chemistry2014

Protein S-nitrosylation: specificity and identification strategies in plants.

Olivier Lamotte, Jean B Bertoldo, Angélique Besson-Bard, Claire Rosnoblet, Sébastien Aimé, Siham Hichami, Hernán Terenzi, David Wendehenne

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
6.1field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

31 citing papers in PubMed, 112 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. De-nitrosylation Coordinates Appressorium Function for Infection of the Rice Blast Fungus.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. S-Nitrosation ofFrontiers in plant science · 2022
    Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Review
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 2 countries.

Olivier LamotteCNRS, UMR 1347 Agroécologie Dijon, France ; ERL CNRS 6300 Dijon, France.
Jean B BertoldoDepartamento de Bioquímica Centro de Ciências Biológicas, Centro de Biologia Molecular Estrutural, Universidade Federal de Santa Catarina Florianópolis, Brasil.
Angélique Besson-BardERL CNRS 6300 Dijon, France ; Université de Bourgogne, UMR 1347 Agroécologie Dijon, France.
Claire RosnobletERL CNRS 6300 Dijon, France ; Université de Bourgogne, UMR 1347 Agroécologie Dijon, France.
Sébastien AiméERL CNRS 6300 Dijon, France ; Institut National de la Recherche Agronomique, UMR 1347 Agroécologie Dijon, France.
Siham HichamiERL CNRS 6300 Dijon, France ; Université de Bourgogne, UMR 1347 Agroécologie Dijon, France.
Hernán TerenziDepartamento de Bioquímica Centro de Ciências Biológicas, Centro de Biologia Molecular Estrutural, Universidade Federal de Santa Catarina Florianópolis, Brasil.
David WendehenneERL CNRS 6300 Dijon, France ; Université de Bourgogne, UMR 1347 Agroécologie Dijon, France.
Centre National de la Recherche Scientifique · FRUniversidade Federal de Santa Catarina · BRUniversité de Bourgogne · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The role of nitric oxide (NO) as a major regulator of plant physiological functions has become increasingly evident. To further improve our understanding of its role, within the last few years plant biologists have begun to embrace the exciting opportunity of investigating protein S-nitrosylation, a major reversible NO-dependent post-translational modification (PTM) targeting specific Cys residues and widely studied in animals. Thanks to the development of dedicated proteomic approaches, in particular the use of the biotin switch technique (BST) combined with mass spectrometry, hundreds of plant protein candidates for S-nitrosylation have been identified. Functional studies focused on specific proteins provided preliminary comprehensive views of how this PTM impacts the structure and function of proteins and, more generally, of how NO might regulate biological plant processes. The aim of this review is to detail the basic principle of protein S-nitrosylation, to provide information on the biochemical and structural features of the S-nitrosylation sites and to describe the proteomic strategies adopted to investigate this PTM in plants. Limits of the current approaches and tomorrow's challenges are also discussed.

Indexed as

biotin switch techniquenitric oxideplantspost-translational modificationssignalingS-nitrosylation

Identifiers

PMID25750911
PMCPMC4285867
OpenAlexW2084529953

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.